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Volume 133, Issue 4

Effect of Ethanol on Activity of the Plasma-membrane ATPase in, and Accumulation of Glycine by, Free

Abstract

SUMMARY: The pH optimum of the ATPase activity in plasma membranes from NCYC 431 from 8 h cultures was around 65 and that in membranes from organisms from 16 h cultures near 6·0. The [ATP] of the enzyme was virtually unaffected by the age of the culture from which organisms were harvested, although the of the enzyme in membranes from organisms from 8 h cultures was higher than that for organisms from 16 h cultures. Ethanol noncompetitively inhibited ATPase activity in membranes, although the inhibition constant for the enzyme from organisms from 8 h cultures was lower than that from organisms from 16 h cultures. Glycine accumulation by the general amino acid permease was non-competitively inhibited by ethanol. Inhibition constants were virtually the same for glycine uptake by deenergized organisms from 8 h and 16 h cultures, but under energized conditions the value was greater for organisms from 16 h rather than 8 h cultures. The data indicate that inhibition of plasma-membrane ATPase activity by ethanol could account, at least in part, for inhibition of glycine accumulation by ethanol.

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© Society for General Microbiology 1987
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1987-04-01
2024-04-24
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Effect of Ethanol on Activity of the Plasma-membrane ATPase in, and Accumulation of Glycine by, Saccharomyces Cerevisiae
Microbiology 133, 857 (1987); https://doi.org/10.1099/00221287-133-4-857
/content/journal/micro/10.1099/00221287-133-4-857
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